The sugar moiety of bovine S-antigen
作者:
ShichiHitoshi,
KochKeith A.,
期刊:
Current Eye Research
(Taylor Available online 1990)
卷期:
Volume 9,
issue sup1
页码: 103-109
ISSN:0271-3683
年代: 1990
DOI:10.3109/02713689008999428
出版商: Taylor&Francis
数据来源: Taylor
摘要:
To obtain insight into the glycoprotein nature of S-antigen (S-Ag), we have investigated the affinity of bovineS-Ag for plant lectins, location of the sugar moiety within the molecule, and incorporation of radiolabelled mannose and glucosamine into S-Ag. It was found (i) that only about 10% of purified S-Ag was bound to concanavalin A (Con A) and wheat germ agglutinin (WGA) columns, (ii) that both concanavalin A and wheat germ agglutinin bound chymotryptic peptides derived from the C-terminal half of S-Ag, and (iii) that radiolabelled D-mannose and D-glucosamine were incorporated into S-Ag and the incorporation was inhibited by tunicamycin, an N-glycosylation inhibitor.14C-Mannose-labelled S-Ag was identified by affinity chromatography on an anti-S-Ag antibody column. These results support the supposition that only a small population of S-Ag is glycosylated (probably in N glycosylated form), and the sugar moiety is located in the C-terminal half of the molecule.
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